Information on EC 1.1.2.B5 - PQQ-dependent quinohemoprotein pyranose dehydrogenase

Substrates: no activity toward common monosaccharides, such as D-glucose, D-fructose, and cellobiose
Products: -

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

heme

2 entries

heme b

739998, 741228

pyrroloquinoline quinone

3 entries

heme

A8P0V4

pyrroloquinoline quinone-dependent quinohemoprotein

heme

quinohemoprotein

pyrroloquinoline quinone

739998, 741228

pyrroloquinoline quinone

pyrroloquinoline quinone-dependent enzyme. The enzyme binds to pyrroloquinoline quinone at a ratio of 1: 1

pyrroloquinoline quinone

A8P0V4

pyrroloquinoline quinone-dependent quinohemoprotein

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Ca2+

1 mM Ca2+ is used in assay conditions

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

30.3

D-arabinose

at pH 8.5 and 30°C

7.9

D-glucosone

at pH 8.5 and 30°C

66.8

D-Lyxose

at pH 8.5 and 30°C

23.1

D-talose

at pH 8.5 and 30°C

3.3 - 6.1

ferricytochrome c

2 entries

24.8

L-fucose

at pH 8.5 and 30°C

49.7

L-galactose

at pH 8.5 and 30°C

363

L-Glucose

at pH 8.5 and 30°C

84.7

L-gulose

at pH 8.5 and 30°C

236

L-Xylose

at pH 8.5 and 30°C

3.3

ferricytochrome c

at pH 6.0 and 30°C

6.1

ferricytochrome c

at pH 8.5 and 30°C

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

35.5

D-arabinose

at pH 8.5 and 30°C

74.1

D-glucosone

at pH 8.5 and 30°C

12.9

D-Lyxose

at pH 8.5 and 30°C

17.8

D-talose

at pH 8.5 and 30°C

30.7 - 53.5

ferricytochrome c

2 entries

56.4

L-fucose

at pH 8.5 and 30°C

56.1

L-galactose

at pH 8.5 and 30°C

24.9

L-Glucose

at pH 8.5 and 30°C

53.3

L-gulose

at pH 8.5 and 30°C

22.4

L-Xylose

at pH 8.5 and 30°C

30.7

ferricytochrome c

at pH 6.0 and 30°C

53.5

ferricytochrome c

at pH 8.5 and 30°C

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kcat/KM VALUE [1/mMs^-1]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

1.17

D-arabinose

at pH 8.5 and 30°C

9.37

D-glucosone

at pH 8.5 and 30°C

0.19

D-Lyxose

at pH 8.5 and 30°C

0.77

D-talose

at pH 8.5 and 30°C

2.27

L-fucose

at pH 8.5 and 30°C

1.13

L-galactose

at pH 8.5 and 30°C

0.07

L-Glucose

at pH 8.5 and 30°C

0.63

L-gulose

at pH 8.5 and 30°C

0.09

L-Xylose

at pH 8.5 and 30°C

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

optimum pH for theoxidation reaction of L-fucose, the electron is directly transferred from the PQQ domain to the electron acceptor. At 8.5 the electron is transferred via the cytochrome domain. This phenomenon indicates that inter-domain electron transfer (IET) is strongly dependent on pH

6.5

for reduction of phenazine methosulfate

8.5

for reduction of ferricytochrome c

show all columns Go to Pi Value Search

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pI VALUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

7.7

calculated from sequence

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only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

Coprinopsis cinerea ATCC MYA-4618

4 entries

A8P0V4

UniProt

brenda

brenda

UniProt

brenda

brenda

formally known as Coprinus cinereus

brenda

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Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

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UNIPROT

ENTRY NAME

ORGANISM

NO. OF AA

NO. OF TRANSM. HELICES

MOLECULAR WEIGHT[Da]

SOURCE

SEQUENCE

LOCALIZATION PREDICTION

The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).

A8P0V4 pBLAST

A8P0V4_COPC7

Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)

726

78379

TrEMBL

Show Sequence

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

98000

SDS-PAGE

Go to Crystallization (commentary) Search

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

sitting drop vapor diffusion method, crystal structure of the catalytic and cytochrome b domains

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

Go to Cloned (commentary) Search

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

expressed in Pichia pastoris

expression in Pichia pastoris

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

diagnostics

bioelectrochemical applications (an amperometric biosensor) in electrochemical devices, based on direct electron transfer reactions. Development of a biosensor to detect urinary L-fucose

top print hide References Search

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

Takeda, K.; Matsumura, H.; Ishida, T.; Yoshida, M.; Igarashi, K.; Samejima, M.; Ohno, H.; Nakamura, N.

pH-dependent electron transfer reaction and direct bioelectrocatalysis of the quinohemoprotein pyranose dehydrogenase

Biochem. Biophys. Res. Commun.

477

369-373

2016

Coprinopsis cinerea

27338639

brenda

Takeda, K.; Matsumura, H.; Ishida, T.; Samejima, M.; Ohno, H.; Yoshida, M.; Igarashi, K.; Nakamura, N.

Characterization of a novel PQQ-dependent quinohemoprotein pyranose dehydrogenase from Coprinopsis cinerea classified into auxiliary activities family 12 in carbohydrate-active enzymes

PLoS ONE

e0115722

2015

Coprinopsis cinerea

25679509

brenda

Takeda, K.; Ishida, T.; Yoshida, M.; Samejima, M.; Ohno, H.; Igarashi, K.; Nakamura, N.

Crystal structure of the catalytic and cytochrome b domains in a eukaryotic pyrroloquinoline quinone-dependent dehydrogenase

Appl. Environ. Microbiol.

e01692-19

2019

Coprinopsis cinerea (A8P0V4), Coprinopsis cinerea ATCC MYA-4618 (A8P0V4)

31604769

brenda